ACE2_CANAL
ID ACE2_CANAL Reviewed; 783 AA.
AC Q59RR0; A0A1D8PTH9;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Cell wall transcription factor ACE2;
GN Name=ACE2; OrderedLocusNames=CAALFM_CR07440WA;
GN ORFNames=CaO19.13543, CaO19.6124;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15255906; DOI=10.1111/j.1365-2958.2004.04185.x;
RA Kelly M.T., MacCallum D.M., Clancy S.D., Odds F.C., Brown A.J., Butler G.;
RT "The Candida albicans CaACE2 gene affects morphogenesis, adherence and
RT virulence.";
RL Mol. Microbiol. 53:969-983(2004).
RN [5]
RP FUNCTION.
RX PubMed=16998073; DOI=10.1128/ec.00155-06;
RA Mulhern S.M., Logue M.E., Butler G.;
RT "Candida albicans transcription factor Ace2 regulates metabolism and is
RT required for filamentation in hypoxic conditions.";
RL Eukaryot. Cell 5:2001-2013(2006).
RN [6]
RP FUNCTION.
RX PubMed=18843050; DOI=10.1091/mbc.e08-03-0272;
RA Song Y., Cheon S.A., Lee K.E., Lee S.Y., Lee B.K., Oh D.B., Kang H.A.,
RA Kim J.Y.;
RT "Role of the RAM network in cell polarity and hyphal morphogenesis in
RT Candida albicans.";
RL Mol. Biol. Cell 19:5456-5477(2008).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=19528234; DOI=10.1128/mcb.01502-08;
RA Wang A., Raniga P.P., Lane S., Lu Y., Liu H.;
RT "Hyphal chain formation in Candida albicans: Cdc28-Hgc1 phosphorylation of
RT Efg1 represses cell separation genes.";
RL Mol. Cell. Biol. 29:4406-4416(2009).
RN [8]
RP FUNCTION.
RX PubMed=21335533; DOI=10.1128/ec.00289-10;
RA Stichternoth C., Fraund A., Setiadi E., Giasson L., Vecchiarelli A.,
RA Ernst J.F.;
RT "Sch9 kinase integrates hypoxia and CO2 sensing to suppress hyphal
RT morphogenesis in Candida albicans.";
RL Eukaryot. Cell 10:502-511(2011).
RN [9]
RP FUNCTION.
RX PubMed=22359502; DOI=10.1371/journal.ppat.1002525;
RA Finkel J.S., Xu W., Huang D., Hill E.M., Desai J.V., Woolford C.A.,
RA Nett J.E., Taff H., Norice C.T., Andes D.R., Lanni F., Mitchell A.P.;
RT "Portrait of Candida albicans adherence regulators.";
RL PLoS Pathog. 8:E1002525-E1002525(2012).
RN [10]
RP FUNCTION.
RX PubMed=23243062; DOI=10.1128/ec.00278-12;
RA Heilmann C.J., Sorgo A.G., Mohammadi S., Sosinska G.J., de Koster C.G.,
RA Brul S., de Koning L.J., Klis F.M.;
RT "Surface stress induces a conserved cell wall stress response in the
RT pathogenic fungus Candida albicans.";
RL Eukaryot. Cell 12:254-264(2013).
CC -!- FUNCTION: Transcription factor involved in the RAM (regulation of ACE2
CC transcription factor and polarized morphogenesis) signaling network
CC that regulates polarized morphogenesis. Regulates expression of genes
CC involved in cell separation such as CHT3, DSE1, and SCW11; or other
CC cell wall genes such as ASH1, DSE4, PIR1, PRY2, and RME1. Required for
CC regulation of morphogenesis, cell separation, adherence, biofilm
CC formation, invasion, as well as virulence in a mouse model of
CC infection. {ECO:0000269|PubMed:15255906, ECO:0000269|PubMed:16998073,
CC ECO:0000269|PubMed:18843050, ECO:0000269|PubMed:21335533,
CC ECO:0000269|PubMed:22359502, ECO:0000269|PubMed:23243062}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15255906,
CC ECO:0000269|PubMed:19528234}. Note=Localized in the nuclei of daughter
CC cells.
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DR EMBL; CP017630; AOW31437.1; -; Genomic_DNA.
DR RefSeq; XP_712331.2; XM_707238.2.
DR AlphaFoldDB; Q59RR0; -.
DR SMR; Q59RR0; -.
DR BioGRID; 1229088; 10.
DR STRING; 237561.Q59RR0; -.
DR PRIDE; Q59RR0; -.
DR GeneID; 3646034; -.
DR KEGG; cal:CAALFM_CR07440WA; -.
DR CGD; CAL0000191878; ACE2.
DR VEuPathDB; FungiDB:CR_07440W_A; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_022817_0_0_1; -.
DR InParanoid; Q59RR0; -.
DR OrthoDB; 1015026at2759; -.
DR PHI-base; PHI:331; -.
DR PRO; PR:Q59RR0; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 4: Predicted;
KW Cell adhesion; Cell wall biogenesis/degradation; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Virulence; Zinc; Zinc-finger.
FT CHAIN 1..783
FT /note="Cell wall transcription factor ACE2"
FT /id="PRO_0000422792"
FT ZN_FING 649..673
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 679..701
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 166..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 90571 MW; 8256A2F177F761A0 CRC64;
MHWKFSNFRK YHLSFHLNLF DLSLFFISFY CFPILYICFF NQVHSFRSTQ PSLIMNKFDL
FDDYSTKGST IPLPNENFDQ LFLSSEANDM EFLFNETLMG LQDLDVPSGY GIPQNTINND
FQHTPNKSKS HSRQYSGTAI FGFADHNKDL SINGVNNDLC KQSNKAINTQ SVSPGELLKR
SRGSQTPTPT SALPDTAQDI LDFNFEEKPI LLLEEDELEE EKHKQQQRMM TQSSPLKRVT
TPSQSPFVQQ PQTMKQRKPH KKTNEYIVAN ENPNSYKFPP SPSPTAKRQQ YPPSSPIPYN
PKSDSVGGNS YSAKYLQSLN KTQQIEYVDD IEPLLQEDNN NMKYIPIPVQ EPMSYQKQKP
VTPPLQSQND SQQLEPLKTP QPQPKQQQQQ QQPNNEQDKE FTANFNFNTF LPPPTPPNLI
NGSPDWNSSP EPHSPSPGRL QPPQQISPIH QNLGAMGNNI NFYTPMYYEL PVQAEQPQPQ
PQPHQQQHQQ QQHQPELQNT YQQIKHIQQQ QQMLQHQFHN QNNQLRQQHP NQFQNQNQNQ
NQNQTKTPYS QQSQFSPTHS NFNLSPAKQL NSNVGSMHLS PLKKQLPNTP TKQPPVTIEW
SPVISPNSKQ PLHKQIKESS PRRRIKKTSL LPPGELDNYW TGPDEDKIYT CTYKNCGKKF
TRRYNVRSHI QTHLSDRPFG CQFCPKRFVR QHDLNRHVKG HIEARYSKCP CGKEFARLDA
LRKHQDRNIC VGGNKNVISK PTKKKGTNNT QQQLLKTDTV VERIEKQLLQ EDKSVTEEFL
MLQ